Literature summary for 1.4.3.19 extracted from

Molla, G.; Motteran, L.; Job, V.; Pilone, M.S.; Pollegioni, L.
Kinetic mechanisms of glycine oxidase from Bacillus subtilis (2003), Eur. J. Biochem., 270, 1474-1482.

Search for more literature for 1.4.3.19

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.38	-	O2	reaction with Gly	Bacillus subtilis
0.42	-	O2	reaction with sarcosine	Bacillus subtilis
0.44	-	O2	reaction with D-Pro	Bacillus subtilis
2.6	-	sarcosine	-	Bacillus subtilis
3.8	-	Gly	-	Bacillus subtilis
76.5	-	D-Pro	-	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
glycine + H2O + O2 = glyoxylate + NH3 + H2O2	ternary complex sequential mechanism	Bacillus subtilis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-Pro + H2O + O2	-	Bacillus subtilis	? + NH3 + H2O2	-	?
glycine + H2O + O2	-	Bacillus subtilis	glyoxylate + NH3 + H2O2	-	?
additional information	glycine oxidase is converted to a two-electron reduced form upon anaerobic reduction with the individual substrates and its reductive half-reaction is reversible	Bacillus subtilis	?	-	?
sarcosine + H2O + O2	-	Bacillus subtilis	glyoxylate + methylamine + H2O2	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
3.5	-	D-Pro	-	Bacillus subtilis
4	-	Gly	-	Bacillus subtilis
4.2	-	sarcosine	-	Bacillus subtilis

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Release 2023.1 (January 2023)